Crystallization of recombinant Crithidia fasciculata tryparedoxin.
J Struct Biol
; 126(1): 76-9, 1999 Jun 01.
Article
em En
| MEDLINE
| ID: mdl-10329491
Recombinant tryparedoxin, a thioredoxin homologue from Crithidia fasciculata, has been purified from an Escherichia coli expression system and used in crystallization trials. Orthorhombic needles in space group P212121, with unit cell dimensions of a = 38.63, b = 51. 47, and c = 73.41 A, have been obtained. The crystals present a monomer of approximate molecular mass 16 kDa in the asymmetric unit and diffract to 1.8-A resolution using synchrotron radiation. Structure determination will be carried out to further the understanding of the role tryparedoxin plays in regulating oxidative stress in parasitic trypanosomatids.
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Base de dados:
MEDLINE
Assunto principal:
Tiorredoxinas
/
Proteínas de Protozoários
Limite:
Animals
Idioma:
En
Revista:
J Struct Biol
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
1999
Tipo de documento:
Article
País de afiliação:
Reino Unido